Analytical Data
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Gene name
ME2
- Application
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P23368
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Expression Region
Gly220~Ala426
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Molecular Weight
27kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
ME2 (Malic Enzyme 2) is an important enzyme in cellular metabolism, primarily involved in the conversion of malate to pyruvate, a reaction that plays a crucial role in the metabolic pathways of energy production and biosynthesis. Research on ME2 has gained prominence due to its involvement in various physiological processes and its implications in several diseases, including metabolic disorders and cancer. Understanding the structure and functionality of ME2 can provide insights into its regulatory mechanisms and the potential development of therapeutic interventions. Recombinant protein studies of ME2 allow for in-depth analysis of its enzymatic properties, interaction with other biomolecules, and its role in metabolic pathways. Furthermore, as ME2 is associated with the modulation of reactive oxygen species and the tricarboxylic acid cycle, its investigation could illuminate the intricacies of cellular respiration and oxidative stress responses. By utilizing techniques such as gene cloning, expression in suitable host systems, and purification, researchers aim to elucidate the enzyme's kinetic parameters and mechanism of action. As the understanding of ME2 expands, it may reveal novel targets for drug development and offer strategies for combating certain metabolic diseases, thus underscoring the significance of ME2 recombinant protein studies in contemporary biomedical research.
